Understand more about biomolecular characteristics, mechanisms and interactions

Advance your research, publish with confidence

Detect changes in secondary and tertiary structure

Today, the sensitivity and accuracy of Chirascan CD spectrometers reveals far more about changes that occur in the higher order structure (HOS) of proteins and other biomolecules when compared to the estimates of α-helix:β-sheet in secondary structure for which circular dichroism was first applied.

From confirming structural integrity to detecting minor changes in secondary and tertiary structure scientists can determine the effect of site-directed mutations on folding/unfolding (stability), monitor response to changes in temperature or pH, and reveal the effect of denaturing agents or binding partners.

Although providing less specific structural information when compared to X-ray crystallography or NMR spectroscopy (both give atomic resolution data), CD analysis offers a rapid analysis of proteins while in solution and requires relatively small amounts of sample.

By enabling the determination of structural and thermodynamic properties, each CD analysis leads to a deeper understanding of biomolecular characteristics, mechanisms and interactions

Gain insight by detecting change

Gain insight and detect changes in secondary and tertiary structure

  • Detect minor differences under native or stressed conditions
  • Characterize protein stability
    • Determine response to thermal or chemical changes
    • Determine structural and thermodynamic properties
    • Study folding and unfolding mechanisms

Secondary structure: far-UV
spectrum of a globular protein

Simultaneous acquisition of CD and absorbance spectra, 0.5 mm pathlength, Chirascan V100. Courtesy of leading research university, Germany

Tertiary structure: near-UV spectra
of two monoclonal antibodies

Differences between near-UV spectra due to slight changes in orientation of aromatic moieties, Chirascan V100, 10 mm pathlength